Effects of magnesium and related divalent metal ions in topoisomerase structure and function
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[1] Sandra J. Aedo,et al. Inhibition of Mg2+ binding and DNA religation by bacterial topoisomerase I via introduction of an additional positive charge into the active site region , 2008, Nucleic acids research.
[2] C. Klee,et al. Calcium as a cellular regulator , 1999 .
[3] S. Kerwin,et al. Synthesis, metal ion binding, and biological evaluation of new anticancer 2-(2'-hydroxyphenyl)benzoxazole analogs of UK-1. , 2008, Bioorganic & medicinal chemistry.
[4] G. Capranico,et al. Anthracyclines: selected new developments. , 2001, Current medicinal chemistry. Anti-cancer agents.
[5] H. Hiasa. The Glu-84 of the ParC subunit plays critical roles in both topoisomerase IV-quinolone and topoisomerase IV-DNA interactions. , 2002, Biochemistry.
[6] Y. Tse‐Dinh,et al. Mechanistic studies on E. coli DNA topoisomerase I: divalent ion effects. , 1991, Journal of inorganic biochemistry.
[7] Y. Tse‐Dinh,et al. Cleavage of dT8 and dT8 phosphorothioyl analogues by Escherichia coli DNA topoisomerase I: product and rate analysis. , 1988, Biochemistry.
[8] N. Osheroff. Eukaryotic topoisomerase II. Characterization of enzyme turnover. , 1986, The Journal of biological chemistry.
[9] M. Palumbo,et al. DNA gyrase requires DNA for effective two-site coordination of divalent metal ions: further insight into the mechanism of enzyme action. , 2008, Biochemistry.
[10] M. Palumbo,et al. The quinolone family: from antibacterial to anticancer agents. , 2003, Current medicinal chemistry. Anti-cancer agents.
[11] M. Palumbo,et al. The effects of metal ions on the structure and stability of the DNA gyrase B protein. , 2005, Journal of molecular biology.
[12] Y. Tse‐Dinh,et al. Mutation adjacent to the active site tyrosine can enhance DNA cleavage and cell killing by the TOPRIM Gly to Ser mutant of bacterial topoisomerase I , 2007, Nucleic acids research.
[13] Jae Young Lee,et al. Making and breaking nucleic acids: two-Mg2+-ion catalysis and substrate specificity. , 2006, Molecular cell.
[14] T. Ceska,et al. A helical arch allowing single-stranded DNA to thread through T5 5'-exonuclease , 1996, Nature.
[15] Y. Tse‐Dinh. Exploring DNA topoisomerases as targets of novel therapeutic agents in the treatment of infectious diseases. , 2007, Infectious disorders drug targets.
[16] G. Ireton,et al. Biochemical and Biophysical Analyses of Recombinant Forms of Human Topoisomerase I (*) , 1996, The Journal of Biological Chemistry.
[17] J. Cowan,et al. Mechanism of metal-promoted catalysis of nucleic acid hydrolysis by Escherichia coli ribonuclease H , 1996, JBIC Journal of Biological Inorganic Chemistry.
[18] Robert J.P. Williams,et al. The Biological Chemistry of the Elements: The Inorganic Chemistry of Life , 2001 .
[19] Y. Tse‐Dinh,et al. Effect of Mg(II) Binding on the Structure and Activity ofEscherichia coli DNA Topoisomerase I* , 1997, The Journal of Biological Chemistry.
[20] K. West,et al. Mutagenesis of E477 or K505 in the B' domain of human topoisomerase II beta increases the requirement for magnesium ions during strand passage. , 2000, Biochemistry.
[21] J. Koeller,et al. Mitoxantrone: a novel anthracycline derivative. , 1988, Clinical pharmacy.
[22] S. Mukhopadhyay,et al. Bacterial Cell Killing Mediated by Topoisomerase I DNA Cleavage Activity* , 2005, Journal of Biological Chemistry.
[23] A. Jeltsch,et al. Structure and function of type II restriction endonucleases. , 2001, Nucleic acids research.
[24] Wei Yang,et al. An equivalent metal ion in one- and two-metal-ion catalysis , 2008, Nature Structural &Molecular Biology.
[25] J. Cowan,et al. Structural and catalytic roles for divalent magnesium in nucleic acid biochemistry , 2002, Biometals.
[26] G. S. Manning. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides , 1978, Quarterly Reviews of Biophysics.
[27] S. Shuman,et al. Mechanistic plasticity of DNA topoisomerase IB: phosphate electrostatics dictate the need for a catalytic arginine. , 2005, Structure.
[28] D. Williams,et al. The Biological Chemistry of the Elements , 1991 .
[29] J. Perona,et al. DNA cleavage by EcoRV endonuclease: two metal ions in three metal ion binding sites. , 2004, Biochemistry.
[30] J. Steitz,et al. A general two-metal-ion mechanism for catalytic RNA. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[31] N. Cozzarelli,et al. The binding of gyrase to DNA: analysis by retention by nitrocellulose filters. , 1982, Nucleic acids research.
[32] N. Osheroff,et al. Human topoisomerase IIα uses a two-metal-ion mechanism for DNA cleavage , 2008, Nucleic acids research.
[33] J. Tainer,et al. Three Metal Ions Participate in the Reaction Catalyzed by T5 Flap Endonuclease* , 2008, Journal of Biological Chemistry.
[34] Charles W. Bock,et al. Manganese as a Replacement for Magnesium and Zinc: Functional Comparison of the Divalent Ions , 1999 .
[35] N. Osheroff. Role of the divalent cation in topoisomerase II mediated reactions. , 1987, Biochemistry.
[36] G. Charles Dismukes,et al. Manganese Enzymes with Binuclear Active Sites. , 1996, Chemical reviews.
[37] James C. Wang,et al. Identification of Active Site Residues in Escherichia coli DNA Topoisomerase I* , 1998, The Journal of Biological Chemistry.
[38] M. Markowitz,et al. Raltegravir (MK-0518): an integrase inhibitor for the treatment of HIV-1. , 2007, Drugs of today.
[39] C. Schein,et al. A “moving metal mechanism” for substrate cleavage by the DNA repair endonuclease APE‐1 , 2007, Proteins.
[40] A. Mildvan,et al. Vaccinia DNA topoisomerase I: single-turnover and steady-state kinetic analysis of the DNA strand cleavage and ligation reactions. , 1994, Biochemistry.
[41] L. Liu,et al. Role of topoisomerase II in mediating epipodophyllotoxin-induced DNA cleavage. , 1984, Cancer research.
[42] J. Berger,et al. DNA topoisomerases: harnessing and constraining energy to govern chromosome topology , 2008, Quarterly Reviews of Biophysics.
[43] J. Cowan. Structural and catalytic chemistry of magnesium-dependent enzymes , 2002, Biometals.
[44] T. Mueser,et al. Structure of Bacteriophage T4 RNase H, a 5′ to 3′ RNA–DNA and DNA–DNA Exonuclease with Sequence Similarity to the RAD2 Family of Eukaryotic Proteins , 1996, Cell.
[45] A. Maxwell,et al. The role of GyrB in the DNA cleavage-religation reaction of DNA gyrase: a proposed two metal-ion mechanism. , 2002, Journal of molecular biology.
[46] L. Hurley,et al. Structural Insight into a Quinolone-Topoisomerase II-DNA Complex , 1999, The Journal of Biological Chemistry.
[47] J. Cowan,et al. Metal Activation of Enzymes in Nucleic Acid Biochemistry. , 1998, Chemical reviews.
[48] Y. Tse‐Dinh. Bacterial and archeal type I topoisomerases. , 1998, Biochimica et biophysica acta.
[49] Carmay Lim,et al. Mononuclear versus binuclear metal-binding sites: metal-binding affinity and selectivity from PDB survey and DFT/CDM calculations. , 2008, Journal of the American Chemical Society.
[50] J. Berger,et al. Structural basis for gate-DNA recognition and bending by type IIA topoisomerases , 2007, Nature.
[51] J. Kuriyan,et al. A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases. , 2000, Journal of molecular biology.
[52] H. Bremer,et al. Winding of the DNA helix by divalent metal ions. , 1997, Nucleic acids research.
[53] Janet M. Thornton,et al. Metal ions in biological catalysis: from enzyme databases to general principles , 2008, JBIC Journal of Biological Inorganic Chemistry.
[54] K. Marx,et al. A gel electrophoresis study of the competitive effects of monovalent counterion on the extent of divalent counterions binding to DNA. , 1998, Biophysical journal.
[55] S. Shuman,et al. Catalytic mechanism of DNA topoisomerase IB. , 2000, Molecular cell.
[56] S. Halford,et al. Divalent metal ions at the active sites of the EcoRV and EcoRI restriction endonucleases. , 1995, Biochemistry.
[57] Y. Tse‐Dinh,et al. The Acidic Triad Conserved in Type IA DNA Topoisomerases Is Required for Binding of Mg(II) and Subsequent Conformational Change* , 2000, The Journal of Biological Chemistry.
[58] Detlef D. Leipe,et al. Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. , 1998, Nucleic acids research.
[59] Chonghui Cheng,et al. Conservation of Structure and Mechanism between Eukaryotic Topoisomerase I and Site-Specific Recombinases , 1998, Cell.
[60] A. Pingoud,et al. Type II restriction endonucleases: structure and mechanism , 2005, Cellular and Molecular Life Sciences.
[61] J. Champoux. DNA topoisomerases: structure, function, and mechanism. , 2001, Annual review of biochemistry.
[62] J. Wang,et al. DNA topoisomerases: why so many? , 1991, The Journal of biological chemistry.
[63] Weiguo Cao,et al. Catalytic mechanism of endonuclease v: a catalytic and regulatory two-metal model. , 2006, Biochemistry.
[64] J. Wang,et al. Structural similarities between topoisomerases that cleave one or both DNA strands. , 1998, Proceedings of the National Academy of Sciences of the United States of America.